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Literature summary for 2.7.7.23 extracted from

  • Zhang, Z.; Tsujimura, M.; Akutsu, J.; Sasaki, M.; Tajima, H.; Kawarabayasi, Y.
    Identification of an extremely thermostable enzyme with dual sugar-1-phosphate nucleotidylyltransferase activities from an acidothermophilic archaeon, Sulfolobus tokodaii strain 7 (2005), J. Biol. Chem., 280, 9698-9705 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BL21-Codon Plus (DE3)-RIL cells Sulfurisphaera tokodaii

Protein Variants

Protein Variants Comment Organism
additional information N-acetyl-D-glucosamine-1-phosphate uridylyltransferase activity of the mutant enzyme deletion mutant lacking the 170-residue C-terminal domain remains in the truncated enzyme after 5 min of heating at 65 °C but is completely removed by treatment over 70°C Sulfurisphaera tokodaii

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ absolute requirement for a divalent cation. The order of effectiveness of metal ions on the activity of the enzyme is Co2+, Mn2+, Mg2+ and Zn2+ Sulfurisphaera tokodaii
Mg2+ absolute requirement for a divalent cation. The order of effectiveness of metal ions on the activity of the enzyme is Co2+, Mn2+, Mg2+ and Zn2+. The optimal Mg2+ concentration is 6 mM, but the enzymatic activity does not change substantially between 2 and 12 mM Sulfurisphaera tokodaii
Mn2+ absolute requirement for a divalent cation. The order of effectiveness of metal ions on the activity of the enzyme is Co2+, Mn2+, Mg2+ and Zn2+ Sulfurisphaera tokodaii
Zn2+ absolute requirement for a divalent cation. The order of effectiveness of metal ions on the activity of the enzyme is Co2+, Mn2+, Mg2+ and Zn2+ Sulfurisphaera tokodaii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate Sulfurisphaera tokodaii
-
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate Sulfurisphaera tokodaii DSM 16993
-
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
?

Organism

Organism UniProt Comment Textmining
Sulfurisphaera tokodaii Q975F9
-
-
Sulfurisphaera tokodaii DSM 16993 Q975F9
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Sulfurisphaera tokodaii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
Sulfurisphaera tokodaii UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
r
diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
Sulfurisphaera tokodaii DSM 16993 UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
r
UTP + alpha-D-glucose 1-phosphate the activity with N-acetyl-D-glucosamine-1-phosphate is 3.4 times higher, respectively, than the corresponding activity with alpha-D-glucose-1-phosphate Sulfurisphaera tokodaii diphosphate + UDP-alpha-D-glucose
-
?
UTP + alpha-D-glucose 1-phosphate the activity with N-acetyl-D-glucosamine-1-phosphate is 3.4 times higher, respectively, than the corresponding activity with alpha-D-glucose-1-phosphate Sulfurisphaera tokodaii DSM 16993 diphosphate + UDP-alpha-D-glucose
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
Sulfurisphaera tokodaii diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate the activity with N-acetyl-D-glucosamine-1-phosphate is 3.4 times higher, respectively, than the corresponding activity with alpha-D-glucose-1-phosphate Sulfurisphaera tokodaii diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
r
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate
-
Sulfurisphaera tokodaii DSM 16993 diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
?
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate the activity with N-acetyl-D-glucosamine-1-phosphate is 3.4 times higher, respectively, than the corresponding activity with alpha-D-glucose-1-phosphate Sulfurisphaera tokodaii DSM 16993 diphosphate + UDP-N-acetyl-alpha-D-glucosamine
-
r

Synonyms

Synonyms Comment Organism
N-acetyl-D-glucosamine-1-phosphate uridylyltransferase
-
Sulfurisphaera tokodaii
ST0452
-
Sulfurisphaera tokodaii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
95
-
-
Sulfurisphaera tokodaii

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
70 100 70°C: about 40% of maximal activity, 100°C: about 80% of maximal activity Sulfurisphaera tokodaii

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
N-acetyl-D-glucosamine-1-phosphate uridylyltransferase activity of the mutant enzyme deletion mutant lacking the 170-residue C-terminal domain remains in the truncated enzyme after 5 min of heating at 65 °C but is completely removed by treatment over 70°C Sulfurisphaera tokodaii
80
-
half-life: 180 min Sulfurisphaera tokodaii
95
-
half-life: 60 min Sulfurisphaera tokodaii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
-
Sulfurisphaera tokodaii

pH Range

pH Minimum pH Maximum Comment Organism
6 10 pH 6.0: about 50% of maximal activity, pH 10.0: about 60% of maximal activity Sulfurisphaera tokodaii